|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02955 |
PLN02955 |
8-amino-7-oxononanoate synthase |
1-476 |
0e+00 |
|
8-amino-7-oxononanoate synthase
Pssm-ID: 178541 [Multi-domain] Cd Length: 476 Bit Score: 1020.76 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573269 1 MADHSWDKTVEEAVNVLESRQILRSLRPICMSRQNEEEIVKSRANGGDGYEVFDGLCQWDRTSVEVSVSIPTFQKWLHDE 80
Cdd:PLN02955 1 MADHSWDKWVEEAVNVLESRQILRSLRPICMSRQNEEEIVKSRANGGDDYEVFDGLCQWDRTSVEVSVSIPTFQKWLHDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573269 81 PSNGEEIFSGDALAECRKGRFKKLLLFSGNDYLGLSSHPTISNAAANAVKEYGMGPKGSALICGYTTYHRLLESSLAQLK 160
Cdd:PLN02955 81 PSNGEEIFSGDALAEERKGRFKKLLLFSGNDYLGLSSHPTISNAAANAAKEYGMGPKGSALICGYTTYHRLLESSLADLK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573269 161 KKEDCLVCPTGFAANMAAMVAIGSVASLLAASGKPLKNEKVAIFSDALNHASIIDGVRLAERQGNVEVFVYRHCDMYHLN 240
Cdd:PLN02955 161 KKEDCLVCPTGFAANMAAMVAIGSVASLLAASGKPLKNEKVAIFSDALNHASIIDGVRLAERQGNVEVFVYRHCDMYHLN 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573269 241 SLLSNCKMKRKVVVTDSLFSMDGDFAPMEELSQLRKKYGFLLVIDDAHGTFVCGENGGGVAEEFNCEADVDLCVGTLSKA 320
Cdd:PLN02955 241 SLLSSCKMKRKVVVTDSLFSMDGDFAPMEELSQLRKKYGFLLVIDDAHGTFVCGENGGGVAEEFNCEADVDLCVGTLSKA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573269 321 AGCHGGFIACSKKWKQLIQSRGRSFIFSTAIPVPMAAAAYAAVVVARKEIWRRKAIWERVKEFKELSGVDISSPIISLVV 400
Cdd:PLN02955 321 AGCHGGFIACSKKWKQLIQSRGRSFIFSTAIPVPMAAAAYAAVVVARKEKWRRKAIWERVKEFKALSGVDISSPIISLVV 400
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 42573269 401 GNQEKALKASRYLLKSGFHVMAIRPPTVPPNSCRLRVTLSAAHTTEDVKKLITALSSCLDFDNTATHIPSFLFPKL 476
Cdd:PLN02955 401 GNQEKALKASRYLLKSGFHVMAIRPPTVPPNSCRLRVTLSAAHTTEDVKKLITALSSCLDFDNTATYIPSFLFPKL 476
|
|
| BioF |
COG0156 |
7-keto-8-aminopelargonate synthetase or related enzyme [Coenzyme transport and metabolism]; ... |
102-460 |
2.53e-150 |
|
7-keto-8-aminopelargonate synthetase or related enzyme [Coenzyme transport and metabolism]; 7-keto-8-aminopelargonate synthetase or related enzyme is part of the Pathway/BioSystem: Biotin biosynthesis
Pssm-ID: 439926 [Multi-domain] Cd Length: 385 Bit Score: 433.32 E-value: 2.53e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573269 102 KKLLLFSGNDYLGLSSHPTISNAAANAVKEYGMGPKGSALICGYTTYHRLLESSLAQLKKKEDCLVCPTGFAANMAAmva 181
Cdd:COG0156 37 REVLNFSSNDYLGLANHPRVIEAAAEALDRYGTGSGGSRLVSGTTPLHEELEEELAEFLGKEAALLFSSGYAANLGV--- 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573269 182 igsVASLLaasgkplkNEKVAIFSDALNHASIIDGVRLAerqgNVEVFVYRHCDMYHLNSLLSNCKM-KRKVVVTDSLFS 260
Cdd:COG0156 114 ---ISALA--------GRGDLIFSDELNHASIIDGARLS----GAKVVRFRHNDMDDLERLLKKARAaRRKLIVTDGVFS 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573269 261 MDGDFAPMEELSQLRKKYGFLLVIDDAHGTFVCGENGGGVAEEFNCEADVDLCVGTLSKAAGCHGGFIACSKKWKQLIQS 340
Cdd:COG0156 179 MDGDIAPLPEIVELAEKYGALLYVDDAHGTGVLGETGRGLVEHFGLEDRVDIIMGTLSKALGSSGGFVAGSKELIDYLRN 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573269 341 RGRSFIFSTAIPVPMAAAAYAAVVVARKEIWRRKAIWERVKEFKEL---SGVDI---SSPIISLVVGNQEKALKASRYLL 414
Cdd:COG0156 259 RARPFIFSTALPPAVAAAALAALEILREEPELRERLWENIAYFREGlkeLGFDLgpsESPIVPVIVGDAERALALADALL 338
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 42573269 415 KSGFHVMAIRPPTVPPNSCRLRVTLSAAHTTEDVKKLITALSSCLD 460
Cdd:COG0156 339 ERGIYVSAIRPPTVPKGTARLRITLSAAHTEEDIDRLLEALAEVGK 384
|
|
| KBL_like |
cd06454 |
KBL_like; this family belongs to the pyridoxal phosphate (PLP)-dependent aspartate ... |
102-456 |
7.47e-125 |
|
KBL_like; this family belongs to the pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). The major groups in this CD corresponds to serine palmitoyltransferase (SPT), 5-aminolevulinate synthase (ALAS), 8-amino-7-oxononanoate synthase (AONS), and 2-amino-3-ketobutyrate CoA ligase (KBL). SPT is responsible for the condensation of L-serine with palmitoyl-CoA to produce 3-ketodihydrospingosine, the reaction of the first step in sphingolipid biosynthesis. ALAS is involved in heme biosynthesis; it catalyzes the synthesis of 5-aminolevulinic acid from glycine and succinyl-coenzyme A. AONS catalyses the decarboxylative condensation of l-alanine and pimeloyl-CoA in the first committed step of biotin biosynthesis. KBL catalyzes the second reaction step of the metabolic degradation pathway for threonine converting 2-amino-3-ketobutyrate, to glycine and acetyl-CoA. The members of this CD are widely found in all three forms of life.
Pssm-ID: 99747 [Multi-domain] Cd Length: 349 Bit Score: 367.27 E-value: 7.47e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573269 102 KKLLLFSGNDYLGLSSHPTISNAAANAVKEYGMGPKGSALICGYTTYHRLLESSLAQLKKKEDCLVCPTGFAANMAamva 181
Cdd:cd06454 1 KKVLNFCSNDYLGLANHPEVIEAAKEALDKYGVGAGGSRLISGTSDLHEELEEELAEFHGKEAALVFSSGYAANDG---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573269 182 igsvasLLAAsgkpLKNEKVAIFSDALNHASIIDGVRLAerqgNVEVFVYRHCDMYHLNSLLSN--CKMKRKVVVTDSLF 259
Cdd:cd06454 77 ------VLST----LAGKGDLIISDSLNHASIIDGIRLS----GAKKRIFKHNDMEDLEKLLREarRPYGKKLIVTEGVY 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573269 260 SMDGDFAPMEELSQLRKKYGFLLVIDDAHGTFVCGENGGGVAEEFNCEADVDLCVGTLSKAAGCHGGFIACSKKWKQLIQ 339
Cdd:cd06454 143 SMDGDIAPLPELVDLAKKYGAILFVDEAHSVGVYGPHGRGVEEFGGLTDDVDIIMGTLGKAFGAVGGYIAGSKELIDYLR 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573269 340 SRGRSFIFSTAIPVPMAAAAYAAVVVARKEIWRRKAIWERVKEFKEL---SGVDI----SSPIISLVVGNQEKALKASRY 412
Cdd:cd06454 223 SYARGFIFSTSLPPAVAAAALAALEVLQGGPERRERLQENVRYLRRGlkeLGFPVggspSHIIPPLIGDDPAKAVAFSDA 302
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 42573269 413 LLKSGFHVMAIRPPTVPPNSCRLRVTLSAAHTTEDVKKLITALS 456
Cdd:cd06454 303 LLERGIYVQAIRYPTVPRGTARLRISLSAAHTKEDIDRLLEALK 346
|
|
| bioF |
TIGR00858 |
8-amino-7-oxononanoate synthase; 7-keto-8-aminopelargonic acid synthetase is an alternate name. ... |
102-455 |
1.11e-116 |
|
8-amino-7-oxononanoate synthase; 7-keto-8-aminopelargonic acid synthetase is an alternate name. This model represents 8-amino-7-oxononanoate synthase, the BioF protein of biotin biosynthesis. This model is based on a careful phylogenetic analysis to separate members of this family from 2-amino-3-ketobutyrate and other related pyridoxal phosphate-dependent enzymes. In several species, including Staphylococcus and Coxiella, a candidate 8-amino-7-oxononanoate synthase is confirmed by location in the midst of a biotin biosynthesis operon but scores below the trusted cutoff of this model. [Biosynthesis of cofactors, prosthetic groups, and carriers, Biotin]
Pssm-ID: 273303 [Multi-domain] Cd Length: 360 Bit Score: 346.95 E-value: 1.11e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573269 102 KKLLLFSGNDYLGLSSHPTISNAAANAVKEYGMGPKGSALICGYTTYHRLLESSLAQLKKKEDCLVCPTGFAANMAAMVA 181
Cdd:TIGR00858 16 RRLLNFSSNDYLGLASHPEVIQAAQQGAEQYGAGSTASRLVSGNSPLHEELEEELAEWKGTEAALLFSSGYLANVGVISA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573269 182 igsvasllaasgkpLKNEKVAIFSDALNHASIIDGVRLAErqgnVEVFVYRHCDMYHL-NSLLSNCKMKRKVVVTDSLFS 260
Cdd:TIGR00858 96 --------------LVGKGDLILSDALNHASLIDGCRLSG----ARVRRYRHNDVEHLeRLLEKNRGERRKLIVTDGVFS 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573269 261 MDGDFAPMEELSQLRKKYGFLLVIDDAHGTFVCGENGGGVAEEFN-CEADVDLCVGTLSKAAGCHGGFIACSKKWKQLIQ 339
Cdd:TIGR00858 158 MDGDIAPLPQLVALAERYGAWLMVDDAHGTGVLGEDGRGTLEHFGlKPEPVDIQVGTLSKALGSYGAYVAGSQALIDYLI 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573269 340 SRGRSFIFSTAIPVPMAAAAYAAVVVARKEIWRRKAIWERVKEFKE------LSGVDISSPIISLVVGNQEKALKASRYL 413
Cdd:TIGR00858 238 NRARTLIFSTALPPAVAAAALAALELIQEEPWRREKLLALIARLRAglealgFTLMPSCTPIVPVIIGDNASALALAEEL 317
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 42573269 414 LKSGFHVMAIRPPTVPPNSCRLRVTLSAAHTTEDVKKLITAL 455
Cdd:TIGR00858 318 QQQGIFVGAIRPPTVPAGTSRLRLTLSAAHTPGDIDRLAEAL 359
|
|
| Aminotran_1_2 |
pfam00155 |
Aminotransferase class I and II; |
102-455 |
3.75e-41 |
|
Aminotransferase class I and II;
Pssm-ID: 395103 [Multi-domain] Cd Length: 351 Bit Score: 150.53 E-value: 3.75e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573269 102 KKLLLFSGNDYLGLsshptISNAAANAVKEYGMGpkGSALICGYTTYHRLLESSLAQLK--------KKEDCLVCPTGFA 173
Cdd:pfam00155 1 TDKINLGSNEYLGD-----TLPAVAKAEKDALAG--GTRNLYGPTDGHPELREALAKFLgrspvlklDREAAVVFGSGAG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573269 174 ANMAAMVAIgsvasllaasgkpLKNEKVAIFSDALNHASIIDGVRLAErqgnVEVFVYR-------HCDMYHLNSLLSNc 246
Cdd:pfam00155 74 ANIEALIFL-------------LANPGDAILVPAPTYASYIRIARLAG----GEVVRYPlydsndfHLDFDALEAALKE- 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573269 247 kmKRKVVVTDSLFSMDGDFAPMEELSQLR---KKYGFLLVIDDAHGTFVCGENGGGVAEEFNCEADVDLCVGTLSKAAGC 323
Cdd:pfam00155 136 --KPKVVLHTSPHNPTGTVATLEELEKLLdlaKEHNILLLVDEAYAGFVFGSPDAVATRALLAEGPNLLVVGSFSKAFGL 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573269 324 HG---GFIACSKKWKQLIQSRGRSFIFSTAIPVPMAAAAYAAVVVARKEIWRRKAIWERVKEF-KELSGVDIS-----SP 394
Cdd:pfam00155 214 AGwrvGYILGNAAVISQLRKLARPFYSSTHLQAAAAAALSDPLLVASELEEMRQRIKERRDYLrDGLQAAGLSvlpsqAG 293
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 42573269 395 IISLVVGNQEKALKASRYLLK-SGFHVMAIRPPTVPPnscRLRVTLsAAHTTEDVKKLITAL 455
Cdd:pfam00155 294 FFLLTGLDPETAKELAQVLLEeVGVYVTPGSSPGVPG---WLRITV-AGGTEEELEELLEAI 351
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02955 |
PLN02955 |
8-amino-7-oxononanoate synthase |
1-476 |
0e+00 |
|
8-amino-7-oxononanoate synthase
Pssm-ID: 178541 [Multi-domain] Cd Length: 476 Bit Score: 1020.76 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573269 1 MADHSWDKTVEEAVNVLESRQILRSLRPICMSRQNEEEIVKSRANGGDGYEVFDGLCQWDRTSVEVSVSIPTFQKWLHDE 80
Cdd:PLN02955 1 MADHSWDKWVEEAVNVLESRQILRSLRPICMSRQNEEEIVKSRANGGDDYEVFDGLCQWDRTSVEVSVSIPTFQKWLHDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573269 81 PSNGEEIFSGDALAECRKGRFKKLLLFSGNDYLGLSSHPTISNAAANAVKEYGMGPKGSALICGYTTYHRLLESSLAQLK 160
Cdd:PLN02955 81 PSNGEEIFSGDALAEERKGRFKKLLLFSGNDYLGLSSHPTISNAAANAAKEYGMGPKGSALICGYTTYHRLLESSLADLK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573269 161 KKEDCLVCPTGFAANMAAMVAIGSVASLLAASGKPLKNEKVAIFSDALNHASIIDGVRLAERQGNVEVFVYRHCDMYHLN 240
Cdd:PLN02955 161 KKEDCLVCPTGFAANMAAMVAIGSVASLLAASGKPLKNEKVAIFSDALNHASIIDGVRLAERQGNVEVFVYRHCDMYHLN 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573269 241 SLLSNCKMKRKVVVTDSLFSMDGDFAPMEELSQLRKKYGFLLVIDDAHGTFVCGENGGGVAEEFNCEADVDLCVGTLSKA 320
Cdd:PLN02955 241 SLLSSCKMKRKVVVTDSLFSMDGDFAPMEELSQLRKKYGFLLVIDDAHGTFVCGENGGGVAEEFNCEADVDLCVGTLSKA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573269 321 AGCHGGFIACSKKWKQLIQSRGRSFIFSTAIPVPMAAAAYAAVVVARKEIWRRKAIWERVKEFKELSGVDISSPIISLVV 400
Cdd:PLN02955 321 AGCHGGFIACSKKWKQLIQSRGRSFIFSTAIPVPMAAAAYAAVVVARKEKWRRKAIWERVKEFKALSGVDISSPIISLVV 400
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 42573269 401 GNQEKALKASRYLLKSGFHVMAIRPPTVPPNSCRLRVTLSAAHTTEDVKKLITALSSCLDFDNTATHIPSFLFPKL 476
Cdd:PLN02955 401 GNQEKALKASRYLLKSGFHVMAIRPPTVPPNSCRLRVTLSAAHTTEDVKKLITALSSCLDFDNTATYIPSFLFPKL 476
|
|
| BioF |
COG0156 |
7-keto-8-aminopelargonate synthetase or related enzyme [Coenzyme transport and metabolism]; ... |
102-460 |
2.53e-150 |
|
7-keto-8-aminopelargonate synthetase or related enzyme [Coenzyme transport and metabolism]; 7-keto-8-aminopelargonate synthetase or related enzyme is part of the Pathway/BioSystem: Biotin biosynthesis
Pssm-ID: 439926 [Multi-domain] Cd Length: 385 Bit Score: 433.32 E-value: 2.53e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573269 102 KKLLLFSGNDYLGLSSHPTISNAAANAVKEYGMGPKGSALICGYTTYHRLLESSLAQLKKKEDCLVCPTGFAANMAAmva 181
Cdd:COG0156 37 REVLNFSSNDYLGLANHPRVIEAAAEALDRYGTGSGGSRLVSGTTPLHEELEEELAEFLGKEAALLFSSGYAANLGV--- 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573269 182 igsVASLLaasgkplkNEKVAIFSDALNHASIIDGVRLAerqgNVEVFVYRHCDMYHLNSLLSNCKM-KRKVVVTDSLFS 260
Cdd:COG0156 114 ---ISALA--------GRGDLIFSDELNHASIIDGARLS----GAKVVRFRHNDMDDLERLLKKARAaRRKLIVTDGVFS 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573269 261 MDGDFAPMEELSQLRKKYGFLLVIDDAHGTFVCGENGGGVAEEFNCEADVDLCVGTLSKAAGCHGGFIACSKKWKQLIQS 340
Cdd:COG0156 179 MDGDIAPLPEIVELAEKYGALLYVDDAHGTGVLGETGRGLVEHFGLEDRVDIIMGTLSKALGSSGGFVAGSKELIDYLRN 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573269 341 RGRSFIFSTAIPVPMAAAAYAAVVVARKEIWRRKAIWERVKEFKEL---SGVDI---SSPIISLVVGNQEKALKASRYLL 414
Cdd:COG0156 259 RARPFIFSTALPPAVAAAALAALEILREEPELRERLWENIAYFREGlkeLGFDLgpsESPIVPVIVGDAERALALADALL 338
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 42573269 415 KSGFHVMAIRPPTVPPNSCRLRVTLSAAHTTEDVKKLITALSSCLD 460
Cdd:COG0156 339 ERGIYVSAIRPPTVPKGTARLRITLSAAHTEEDIDRLLEALAEVGK 384
|
|
| KBL_like |
cd06454 |
KBL_like; this family belongs to the pyridoxal phosphate (PLP)-dependent aspartate ... |
102-456 |
7.47e-125 |
|
KBL_like; this family belongs to the pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). The major groups in this CD corresponds to serine palmitoyltransferase (SPT), 5-aminolevulinate synthase (ALAS), 8-amino-7-oxononanoate synthase (AONS), and 2-amino-3-ketobutyrate CoA ligase (KBL). SPT is responsible for the condensation of L-serine with palmitoyl-CoA to produce 3-ketodihydrospingosine, the reaction of the first step in sphingolipid biosynthesis. ALAS is involved in heme biosynthesis; it catalyzes the synthesis of 5-aminolevulinic acid from glycine and succinyl-coenzyme A. AONS catalyses the decarboxylative condensation of l-alanine and pimeloyl-CoA in the first committed step of biotin biosynthesis. KBL catalyzes the second reaction step of the metabolic degradation pathway for threonine converting 2-amino-3-ketobutyrate, to glycine and acetyl-CoA. The members of this CD are widely found in all three forms of life.
Pssm-ID: 99747 [Multi-domain] Cd Length: 349 Bit Score: 367.27 E-value: 7.47e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573269 102 KKLLLFSGNDYLGLSSHPTISNAAANAVKEYGMGPKGSALICGYTTYHRLLESSLAQLKKKEDCLVCPTGFAANMAamva 181
Cdd:cd06454 1 KKVLNFCSNDYLGLANHPEVIEAAKEALDKYGVGAGGSRLISGTSDLHEELEEELAEFHGKEAALVFSSGYAANDG---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573269 182 igsvasLLAAsgkpLKNEKVAIFSDALNHASIIDGVRLAerqgNVEVFVYRHCDMYHLNSLLSN--CKMKRKVVVTDSLF 259
Cdd:cd06454 77 ------VLST----LAGKGDLIISDSLNHASIIDGIRLS----GAKKRIFKHNDMEDLEKLLREarRPYGKKLIVTEGVY 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573269 260 SMDGDFAPMEELSQLRKKYGFLLVIDDAHGTFVCGENGGGVAEEFNCEADVDLCVGTLSKAAGCHGGFIACSKKWKQLIQ 339
Cdd:cd06454 143 SMDGDIAPLPELVDLAKKYGAILFVDEAHSVGVYGPHGRGVEEFGGLTDDVDIIMGTLGKAFGAVGGYIAGSKELIDYLR 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573269 340 SRGRSFIFSTAIPVPMAAAAYAAVVVARKEIWRRKAIWERVKEFKEL---SGVDI----SSPIISLVVGNQEKALKASRY 412
Cdd:cd06454 223 SYARGFIFSTSLPPAVAAAALAALEVLQGGPERRERLQENVRYLRRGlkeLGFPVggspSHIIPPLIGDDPAKAVAFSDA 302
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 42573269 413 LLKSGFHVMAIRPPTVPPNSCRLRVTLSAAHTTEDVKKLITALS 456
Cdd:cd06454 303 LLERGIYVQAIRYPTVPRGTARLRISLSAAHTKEDIDRLLEALK 346
|
|
| PRK05958 |
PRK05958 |
8-amino-7-oxononanoate synthase; Reviewed |
102-459 |
3.05e-124 |
|
8-amino-7-oxononanoate synthase; Reviewed
Pssm-ID: 235655 [Multi-domain] Cd Length: 385 Bit Score: 367.18 E-value: 3.05e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573269 102 KKLLLFSGNDYLGLSSHPTISNAAANAVKEYGMGPKGSALICGYTTYHRLLESSLAQLKKKEDCLVCPTGFAANMAAMVA 181
Cdd:PRK05958 39 RRMLNFASNDYLGLARHPRLIAAAQQAARRYGAGSGGSRLVTGNSPAHEALEEELAEWFGAERALLFSSGYAANLAVLTA 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573269 182 IGSVASLlaasgkplknekvaIFSDALNHASIIDGVRLaerqGNVEVFVYRHCDMYHLNSLLSNCKMKRKVVVTDSLFSM 261
Cdd:PRK05958 119 LAGKGDL--------------IVSDKLNHASLIDGARL----SRARVRRYPHNDVDALEALLAKWRAGRALIVTESVFSM 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573269 262 DGDFAPMEELSQLRKKYGFLLVIDDAHGTFVCGENGGGVAEEFNCEADVD-LCVGTLSKAAGCHGGFIACSKKWKQ-LIQ 339
Cdd:PRK05958 181 DGDLAPLAELVALARRHGAWLLVDEAHGTGVLGPQGRGLAAEAGLAGEPDvILVGTLGKALGSSGAAVLGSETLIDyLIN 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573269 340 sRGRSFIFSTAIPVPMAAAAYAAVVVARKEIWRRKAIWERVKEFKE------LSGVDISSPIISLVVGNQEKALKASRYL 413
Cdd:PRK05958 261 -RARPFIFTTALPPAQAAAARAALRILRREPERRERLAALIARLRAglralgFQLMDSQSAIQPLIVGDNERALALAAAL 339
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 42573269 414 LKSGFHVMAIRPPTVPPNSCRLRVTLSAAHTTEDVKKLITALSSCL 459
Cdd:PRK05958 340 QEQGFWVGAIRPPTVPAGTSRLRITLTAAHTEADIDRLLEALAEAL 385
|
|
| bioF |
TIGR00858 |
8-amino-7-oxononanoate synthase; 7-keto-8-aminopelargonic acid synthetase is an alternate name. ... |
102-455 |
1.11e-116 |
|
8-amino-7-oxononanoate synthase; 7-keto-8-aminopelargonic acid synthetase is an alternate name. This model represents 8-amino-7-oxononanoate synthase, the BioF protein of biotin biosynthesis. This model is based on a careful phylogenetic analysis to separate members of this family from 2-amino-3-ketobutyrate and other related pyridoxal phosphate-dependent enzymes. In several species, including Staphylococcus and Coxiella, a candidate 8-amino-7-oxononanoate synthase is confirmed by location in the midst of a biotin biosynthesis operon but scores below the trusted cutoff of this model. [Biosynthesis of cofactors, prosthetic groups, and carriers, Biotin]
Pssm-ID: 273303 [Multi-domain] Cd Length: 360 Bit Score: 346.95 E-value: 1.11e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573269 102 KKLLLFSGNDYLGLSSHPTISNAAANAVKEYGMGPKGSALICGYTTYHRLLESSLAQLKKKEDCLVCPTGFAANMAAMVA 181
Cdd:TIGR00858 16 RRLLNFSSNDYLGLASHPEVIQAAQQGAEQYGAGSTASRLVSGNSPLHEELEEELAEWKGTEAALLFSSGYLANVGVISA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573269 182 igsvasllaasgkpLKNEKVAIFSDALNHASIIDGVRLAErqgnVEVFVYRHCDMYHL-NSLLSNCKMKRKVVVTDSLFS 260
Cdd:TIGR00858 96 --------------LVGKGDLILSDALNHASLIDGCRLSG----ARVRRYRHNDVEHLeRLLEKNRGERRKLIVTDGVFS 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573269 261 MDGDFAPMEELSQLRKKYGFLLVIDDAHGTFVCGENGGGVAEEFN-CEADVDLCVGTLSKAAGCHGGFIACSKKWKQLIQ 339
Cdd:TIGR00858 158 MDGDIAPLPQLVALAERYGAWLMVDDAHGTGVLGEDGRGTLEHFGlKPEPVDIQVGTLSKALGSYGAYVAGSQALIDYLI 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573269 340 SRGRSFIFSTAIPVPMAAAAYAAVVVARKEIWRRKAIWERVKEFKE------LSGVDISSPIISLVVGNQEKALKASRYL 413
Cdd:TIGR00858 238 NRARTLIFSTALPPAVAAAALAALELIQEEPWRREKLLALIARLRAglealgFTLMPSCTPIVPVIIGDNASALALAEEL 317
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 42573269 414 LKSGFHVMAIRPPTVPPNSCRLRVTLSAAHTTEDVKKLITAL 455
Cdd:TIGR00858 318 QQQGIFVGAIRPPTVPAGTSRLRLTLSAAHTPGDIDRLAEAL 359
|
|
| gly_Cac_T_rel |
TIGR01825 |
pyridoxal phosphate-dependent acyltransferase, putative; This model represents an enzyme ... |
102-454 |
2.85e-80 |
|
pyridoxal phosphate-dependent acyltransferase, putative; This model represents an enzyme subfamily related to three known enzymes; it appears closest to glycine C-acteyltransferase, shows no overlap with it in species distribution, and may share that function. The three closely related enzymes are glycine C-acetyltransferase (2-amino-3-ketobutyrate coenzyme A ligase), 5-aminolevulinic acid synthase, and 8-amino-7-oxononanoate synthase. All transfer the R-group (acetyl, succinyl, or 6-carboxyhexanoyl) from coenzyme A to an amino acid (Gly, Gly, Ala, respectively), with release of CO2 for the latter two reactions.
Pssm-ID: 130884 [Multi-domain] Cd Length: 385 Bit Score: 254.36 E-value: 2.85e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573269 102 KKLLLFSGNDYLGLSSHPTISNAAANAVKEYGMGPKGSALICGYTTYHRLLESSLAQLKKKEDCLVCPTGFAANMAAMVA 181
Cdd:TIGR01825 33 KEVINLSSNNYLGFADHPRLKEAAAQAIQQYGVGAGAVRTIAGTLRLHEELEEKLAKFKKTEAALVFQSGFNTNQGVLSA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573269 182 IGSvasllaasgkplKNEkvAIFSDALNHASIIDGVRLAErqgnVEVFVYRHCDMYHLNSLL-SNCKMKRKVVVTDSLFS 260
Cdd:TIGR01825 113 LLR------------KGD--IVLSDELNHASIIDGLRLTK----ATKKIYKHADMDDLDRVLrENPSYGKKLIVTDGVFS 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573269 261 MDGDFAPMEELSQLRKKYGFLLVIDDAHGTFVCGENGGGVAEEFNCEADVDLCVGTLSKAAGCHGGFIACSKKWKQLIQS 340
Cdd:TIGR01825 175 MDGDVAPLPEIVELAERYGAVTYVDDAHGSGVMGEAGRGTVHHFGLEDKVDIQVGTLSKAIGVVGGYAAGHKELIEYLKN 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573269 341 RGRSFIFSTAIPVPMAAAAYAAVVVARKEIWRRKAIWERVKEFK-ELS--GVDIS---SPIISLVVGNQEKALKASRYLL 414
Cdd:TIGR01825 255 RARPFLFSTAQPPAVVAALAAAVDELQRSPELMERLWDNTRFFKaGLGklGYDTGgseTPITPVVIGDEKAAQEFSRRLF 334
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 42573269 415 KSGFHVMAIRPPTVPPNSCRLRVTLSAAHTTEDVKKLITA 454
Cdd:TIGR01825 335 DEGIFAQSIVFPTVPRGTARIRNIPTAEHTKDDLDQALDA 374
|
|
| PRK06939 |
PRK06939 |
2-amino-3-ketobutyrate coenzyme A ligase; Provisional |
102-454 |
5.86e-80 |
|
2-amino-3-ketobutyrate coenzyme A ligase; Provisional
Pssm-ID: 235893 [Multi-domain] Cd Length: 397 Bit Score: 253.58 E-value: 5.86e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573269 102 KKLLLFSGNDYLGLSSHPTISNAAANAVKEYGMGPKGSALICGYTTYHRLLESSLAQLKKKEDCLVCPTGFAANMAAMva 181
Cdd:PRK06939 42 KEVINFCANNYLGLANHPELIAAAKAALDSHGFGMASVRFICGTQDLHKELEEKLAKFLGTEDAILYSSCFDANGGLF-- 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573269 182 igsvasllaasgKPLKNEKVAIFSDALNHASIIDGVRL--AERqgnvevFVYRHCDMYHLNSLL---SNCKMKRKVVVTD 256
Cdd:PRK06939 120 ------------ETLLGKEDAIISDALNHASIIDGVRLckAKR------YRYANNDMADLEAQLkeaKEAGARHKLIATD 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573269 257 SLFSMDGDFAPMEELSQLRKKYGFLLVIDDAHGTFVCGENGGGVAEEFNCEADVDLCVGTLSKA-AGCHGGFIACSKKWK 335
Cdd:PRK06939 182 GVFSMDGDIAPLPEICDLADKYDALVMVDDSHAVGFVGENGRGTVEHFGVMDRVDIITGTLGKAlGGASGGYTAGRKEVI 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573269 336 QLIQSRGRSFIFSTAIPVPMAAAAYAAVVVARKEIWRRKAIWERVKEFKE-LS--GVDI---SSPIISLVVGNQEKALKA 409
Cdd:PRK06939 262 DWLRQRSRPYLFSNSLAPAIVAASIKVLELLEESDELRDRLWENARYFREgMTaaGFTLgpgEHPIIPVMLGDAKLAQEF 341
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 42573269 410 SRYLLKSGFHVMAIRPPTVPPNSCRLRVTLSAAHTTEDVKKLITA 454
Cdd:PRK06939 342 ADRLLEEGVYVIGFSFPVVPKGQARIRTQMSAAHTKEQLDRAIDA 386
|
|
| 5aminolev_synth |
TIGR01821 |
5-aminolevulinic acid synthase; This model represents 5-aminolevulinic acid synthase, an ... |
102-455 |
2.98e-79 |
|
5-aminolevulinic acid synthase; This model represents 5-aminolevulinic acid synthase, an enzyme for one of two routes to the heme precursor 5-aminolevulinate. The protein is a pyridoxal phosphate-dependent enzyme related to 2-amino-3-ketobutyrate CoA tranferase and 8-amino-7-oxononanoate synthase. This enzyme appears restricted to the alpha Proteobacteria and mitochondrial derivatives. [Biosynthesis of cofactors, prosthetic groups, and carriers, Heme, porphyrin, and cobalamin]
Pssm-ID: 273820 [Multi-domain] Cd Length: 402 Bit Score: 252.34 E-value: 2.98e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573269 102 KKLLLFSGNDYLGLSSHPTISNAAANAVKEYGMGPKGSALICGYTTYHRLLESSLAQLKKKEDCLVCPTGFAANMAAmva 181
Cdd:TIGR01821 45 KDVTVWCSNDYLGMGQHPEVLQAMHETLDKYGAGAGGTRNISGTNIPHVELEAELADLHGKESALVFTSGYVANDAT--- 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573269 182 igsvaslLAASGKPLKNekVAIFSDALNHASIIDGVrlaeRQGNVEVFVYRHCDMYHLNSLLSNCKMKR-KVVVTDSLFS 260
Cdd:TIGR01821 122 -------LATLAKIIPG--CVIFSDELNHASMIEGI----RHSGAEKFIFRHNDVAHLEKLLQSVDPNRpKIIAFESVYS 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573269 261 MDGDFAPMEELSQLRKKYGFLLVIDDAHGTFVCGENGGGVAEEFNCEADVDLCVGTLSKAAGCHGGFIACSKKWKQLIQS 340
Cdd:TIGR01821 189 MDGDIAPIEEICDLADKYGALTYLDEVHAVGLYGPRGGGIAERDGLMHRIDIIEGTLAKAFGVVGGYIAASRKLIDAIRS 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573269 341 RGRSFIFSTAIPVPMAAAAYAAVVVARKEIWRRKAIWERVKEFKE------LSGVDISSPIISLVVGNQEKALKASRYLL 414
Cdd:TIGR01821 269 YAPGFIFTTSLPPAIAAGATASIRHLKESQDLRRAHQENVKRLKNllealgIPVIPNPSHIVPVIIGDAALCKKVSDLLL 348
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 42573269 415 -KSGFHVMAIRPPTVPPNSCRLRVTLSAAHTTEDVKKLITAL 455
Cdd:TIGR01821 349 nKHGIYVQPINYPTVPRGTERLRITPTPAHTDKMIDDLVEAL 390
|
|
| PRK13392 |
PRK13392 |
5-aminolevulinate synthase; Provisional |
97-460 |
4.87e-69 |
|
5-aminolevulinate synthase; Provisional
Pssm-ID: 184023 [Multi-domain] Cd Length: 410 Bit Score: 225.89 E-value: 4.87e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573269 97 RKGRFKKLLLFSGNDYLGLSSHPTISNAAANAVKEYGMGPKGSALICGYTTYHRLLESSLAQLKKKEDCLVCPTGFAANM 176
Cdd:PRK13392 41 GPDGPRRVTIWCSNDYLGMGQHPDVIGAMVDALDRYGAGAGGTRNISGTSHPHVLLERELADLHGKESALLFTSGYVSND 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573269 177 AAmvaIGSVASLLAAsgkplknekVAIFSDALNHASIIDGVRL--AERQgnvevfVYRHCDMYHLNSLLSNCKMKR-KVV 253
Cdd:PRK13392 121 AA---LSTLGKLLPG---------CVILSDALNHASMIEGIRRsgAEKQ------VFRHNDLADLEEQLASVDPDRpKLI 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573269 254 VTDSLFSMDGDFAPMEELSQLRKKYGFLLVIDDAHGTFVCGENGGGVAEEFNCEADVDLCVGTLSKAAGCHGGFIACSKK 333
Cdd:PRK13392 183 AFESVYSMDGDIAPIEAICDLADRYNALTYVDEVHAVGLYGARGGGIAERDGLMDRIDMIQGTLAKAFGCLGGYIAASAD 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573269 334 WKQLIQSRGRSFIFSTAIPVPMAAAAYAAVVVARKEIWRRKAIWERVKEFK-ELSGVDI-----SSPIISLVVGNQEKAL 407
Cdd:PRK13392 263 LIDFVRSFAPGFIFTTALPPAVAAGATAAIRHLKTSQTERDAHQDRVAALKaKLNANGIpvmpsPSHIVPVMVGDPTLCK 342
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 42573269 408 KASRYLLKS-GFHVMAIRPPTVPPNSCRLRVTLSAAHTTEDVKKLITALSSCLD 460
Cdd:PRK13392 343 AISDRLMSEhGIYIQPINYPTVPRGTERLRITPTPLHDDEDIDALVAALVAIWD 396
|
|
| PRK07179 |
PRK07179 |
quorum-sensing autoinducer synthase; |
105-460 |
6.30e-42 |
|
quorum-sensing autoinducer synthase;
Pssm-ID: 180866 [Multi-domain] Cd Length: 407 Bit Score: 154.01 E-value: 6.30e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573269 105 LLFSGNDYLGLSSHPTISNAAANAVKEYGMGPKGSALICGYTTYHRLLESSLAQLKKKEDCLVCPTGFAANMAAMVAIGS 184
Cdd:PRK07179 57 IILQSNDYLNLSGHPDIIKAQIAALQEEGDSLVMSAVFLHDDSPKPQFEKKLAAFTGFESCLLCQSGWAANVGLLQTIAD 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573269 185 vasllaasgkplknEKVAIFSDALNHASIIDGVRLAERQgnveVFVYRHCDMYHLNSLLSncKMKRKVVVTDSLFSMDGD 264
Cdd:PRK07179 137 --------------PNTPVYIDFFAHMSLWEGVRAAGAQ----AHPFRHNDVDHLRRQIE--RHGPGIIVVDSVYSTTGT 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573269 265 FAPMEELSQLRKKYGFLLVIDDAH--GTFvcGENGGGVAEEFNCEADVDLCVGTLSKAAGCHGGFIACSKKWKQLIQSRG 342
Cdd:PRK07179 197 IAPLADIVDIAEEFGCVLVVDESHslGTH--GPQGAGLVAELGLTSRVHFITASLAKAFAGRAGIITCPRELAEYVPFVS 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573269 343 RSFIFSTAIPVPMAAAAYAAVVVARKEIWRRKAIWERVKEFKE-LS--GVDI--SSPIISLVVGNQEKALKASRYLLKSG 417
Cdd:PRK07179 275 YPAIFSSTLLPHEIAGLEATLEVIESADDRRARLHANARFLREgLSelGYNIrsESQIIALETGSERNTEVLRDALEERN 354
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 42573269 418 -FHVMAIRPPTvPPNSCRLRVTLSAAHTTEDVKKLITALSSCLD 460
Cdd:PRK07179 355 vFGAVFCAPAT-PKNRNLIRLSLNADLTASDLDRVLEVCREARD 397
|
|
| Aminotran_1_2 |
pfam00155 |
Aminotransferase class I and II; |
102-455 |
3.75e-41 |
|
Aminotransferase class I and II;
Pssm-ID: 395103 [Multi-domain] Cd Length: 351 Bit Score: 150.53 E-value: 3.75e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573269 102 KKLLLFSGNDYLGLsshptISNAAANAVKEYGMGpkGSALICGYTTYHRLLESSLAQLK--------KKEDCLVCPTGFA 173
Cdd:pfam00155 1 TDKINLGSNEYLGD-----TLPAVAKAEKDALAG--GTRNLYGPTDGHPELREALAKFLgrspvlklDREAAVVFGSGAG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573269 174 ANMAAMVAIgsvasllaasgkpLKNEKVAIFSDALNHASIIDGVRLAErqgnVEVFVYR-------HCDMYHLNSLLSNc 246
Cdd:pfam00155 74 ANIEALIFL-------------LANPGDAILVPAPTYASYIRIARLAG----GEVVRYPlydsndfHLDFDALEAALKE- 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573269 247 kmKRKVVVTDSLFSMDGDFAPMEELSQLR---KKYGFLLVIDDAHGTFVCGENGGGVAEEFNCEADVDLCVGTLSKAAGC 323
Cdd:pfam00155 136 --KPKVVLHTSPHNPTGTVATLEELEKLLdlaKEHNILLLVDEAYAGFVFGSPDAVATRALLAEGPNLLVVGSFSKAFGL 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573269 324 HG---GFIACSKKWKQLIQSRGRSFIFSTAIPVPMAAAAYAAVVVARKEIWRRKAIWERVKEF-KELSGVDIS-----SP 394
Cdd:pfam00155 214 AGwrvGYILGNAAVISQLRKLARPFYSSTHLQAAAAAALSDPLLVASELEEMRQRIKERRDYLrDGLQAAGLSvlpsqAG 293
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 42573269 395 IISLVVGNQEKALKASRYLLK-SGFHVMAIRPPTVPPnscRLRVTLsAAHTTEDVKKLITAL 455
Cdd:pfam00155 294 FFLLTGLDPETAKELAQVLLEeVGVYVTPGSSPGVPG---WLRITV-AGGTEEELEELLEAI 351
|
|
| PRK07505 |
PRK07505 |
hypothetical protein; Provisional |
107-460 |
1.88e-40 |
|
hypothetical protein; Provisional
Pssm-ID: 181006 [Multi-domain] Cd Length: 402 Bit Score: 149.74 E-value: 1.88e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573269 107 FSGNDYLGLSSHPTISNAAANAVKEYGMGPKGSALICGYTTYHRLLESSLAQLKKKEdCLVCPTGFAANMAAMVAIGSva 186
Cdd:PRK07505 51 FVSCSYLGLDTHPAIIEGAVDALKRTGSLHLSSSRTRVRSQILKDLEEALSELFGAS-VLTFTSCSAAHLGILPLLAS-- 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573269 187 SLLAASGKPlknekVAIFsDALNHASIIDGVRLAERQGNVEVfvyrhCDMYHLNSLLSNCKMKRKVV-VTDSLFSMdGDF 265
Cdd:PRK07505 128 GHLTGGVPP-----HMVF-DKNAHASLNILKGICADETEVET-----IDHNDLDALEDICKTNKTVAyVADGVYSM-GGI 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573269 266 APMEELSQLRKKYGFLLVIDDAHGTFVCGENGGGVAEEfncEADVDL-----CVGTLSKAAGCHGGFIAC-SKKWKQLIQ 339
Cdd:PRK07505 196 APVKELLRLQEKYGLFLYIDDAHGLSIYGKNGEGYVRS---ELDYRLnertiIAASLGKAFGASGGVIMLgDAEQIELIL 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573269 340 SRGRSFIFSTAIPVPMAAAAYAAVVVARK-EIWRR-KAIWERVKEFKEL-----SGVdiSSPIISLVVGNQEKALKASRY 412
Cdd:PRK07505 273 RYAGPLAFSQSLNVAALGAILASAEIHLSeELDQLqQKLQNNIALFDSLipteqSGS--FLPIRLIYIGDEDTAIKAAKQ 350
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 42573269 413 LLKSGFHVMAIRPPTVPPNSCRLRVTLSAAHTTEDVKKLITALSSCLD 460
Cdd:PRK07505 351 LLDRGFYTSPVFFPVVAKGRAGLRIMFRASHTNDEIKRLCSLLKEILD 398
|
|
| PLN02483 |
PLN02483 |
serine palmitoyltransferase |
111-460 |
6.36e-30 |
|
serine palmitoyltransferase
Pssm-ID: 178101 [Multi-domain] Cd Length: 489 Bit Score: 121.79 E-value: 6.36e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573269 111 DYLGL-SSHPTISNAAANAVKEYGMGPKGSALICGYTTYHRLLESSLAQLKKKEDCLVCPTGFAANMAAMVAIGSVASLl 189
Cdd:PLN02483 109 NYLGFaAADEYCTPRVIESLKKYSASTCSSRVDGGTTKLHRELEELVARFVGKPAAIVFGMGYATNSTIIPALIGKGGL- 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573269 190 aasgkplknekvaIFSDALNHASIIDGVRLAerqgNVEVFVYRHCDMYHLNSLL----------SNCKMKRKVVVTDSLF 259
Cdd:PLN02483 188 -------------IISDSLNHNSIVNGARGS----GATIRVFQHNTPSHLEEVLreqiaegqprTHRPWKKIIVIVEGIY 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573269 260 SMDGDFAPMEELSQLRKKYGFLLVIDDAHGTFVCGENGGGVAEEFNCE-ADVDLCVGTLSKAAGCHGGFIACSKKWKQLI 338
Cdd:PLN02483 251 SMEGELCKLPEIVAVCKKYKAYVYLDEAHSIGAVGKTGRGVCELLGVDpADVDIMMGTFTKSFGSCGGYIAGSKELIQYL 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573269 339 QSRGRSFIFSTAIPVPMAAAAYAAVVVARKE----IWRRK--AIWERVKEFK-ELSGV------DISSPIISLVVGNQEK 405
Cdd:PLN02483 331 KRTCPAHLYATSMSPPAVQQVISAIKVILGEdgtnRGAQKlaQIRENSNFFRsELQKMgfevlgDNDSPVMPIMLYNPAK 410
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 42573269 406 ALKASRYLLKSGFHVMAIRPPTVPPNSCRLRVTLSAAHTTEDVKKLITALSSCLD 460
Cdd:PLN02483 411 IPAFSRECLKQNVAVVVVGFPATPLLLARARICISASHSREDLIKALEVISEVGD 465
|
|
| PLN03227 |
PLN03227 |
serine palmitoyltransferase-like protein; Provisional |
105-460 |
8.72e-24 |
|
serine palmitoyltransferase-like protein; Provisional
Pssm-ID: 178766 [Multi-domain] Cd Length: 392 Bit Score: 102.68 E-value: 8.72e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573269 105 LLFSGNDYLGLSSHPTISNAAANAVKEYGMGPKGSALICGYTTYHRLLESSLAQLKKKEDCLVCPTGFAANMAAMVAIGS 184
Cdd:PLN03227 1 LNFATHDFLSTSSSPTLRQTALESLSHYGCGSCGPRGFYGTIDAHLELEQCMAEFLGTESAILYSDGASTTSSTVAAFAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573269 185 VASLLAAsgkplknekvaifsDALNHASIIDGVRLAErqgnVEVFVYRHCDMYHLNSLLSNCK-----------MKRKVV 253
Cdd:PLN03227 81 RGDLLVV--------------DRGVNEALLVGVSLSR----ANVRWFRHNDMKDLRRVLEQVRaqdvalkrkptDQRRFL 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573269 254 VTDSLFSMDGDFAPMEELSQLRKKYGFLLVIDDAHGTFVCGENGGGVAEEFNCE--ADVDLCVGTLSKAAGCHGGFIACS 331
Cdd:PLN03227 143 VVEGLYKNTGTLAPLKELVALKEEFHYRLILDESFSFGTLGKSGRGSLEHAGLKpmVHAEIVTFSLENAFGSVGGMTVGS 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573269 332 KKWKQLIQSRGRSFIFSTAIPVPMAAAAYAAVVVARKEiwrrKAIWERVKE-----FKELSGVDIS-------------- 392
Cdd:PLN03227 223 EEVVDHQRLSGSGYCFSASAPPFLAKADATATAGELAG----PQLLNRLHDsianlYSTLTNSSHPyalklrnrlvitsd 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573269 393 --SPIISLVVGNQEKA---------LKASRYLLKSGFHVMAIR------PPTVPPNScrLRVTLSAAHTTEDVKKLITAL 455
Cdd:PLN03227 299 piSPIIYLRLSDQEATrrtdetlilDQIAHHSLSEGVAVVSTGghvkkfLQLVPPPC--LRVVANASHTREDIDKLLTVL 376
|
....*
gi 42573269 456 SSCLD 460
Cdd:PLN03227 377 GEAVE 381
|
|
| PRK05937 |
PRK05937 |
8-amino-7-oxononanoate synthase; Provisional |
107-460 |
6.02e-23 |
|
8-amino-7-oxononanoate synthase; Provisional
Pssm-ID: 102071 [Multi-domain] Cd Length: 370 Bit Score: 99.86 E-value: 6.02e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573269 107 FSGNDYLGLSSHPTISNAAANAVKEY-------GMGPKGSALICGYTTYHRLLESSLAQLKKKEDCLVCPTGFAANMAAM 179
Cdd:PRK05937 9 FVTNDFLGFSRSDTLVHEVEKRYRLYcrqfphaQLGYGGSRAILGPSSLLDDLEHKIAHFHGAPEAFIVPSGYMANLGLC 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573269 180 VAIGSVASLLaasgkplknekvaiFSDALNHASIIDGVRLAERQGNVevfvYRHCDMYHLNSLLSNCKM---KRKVVVTD 256
Cdd:PRK05937 89 AHLSSVTDYV--------------LWDEQVHISVVYSLSVISGWHQS----FRHNDLDHLESLLESCRQrsfGRIFIFVC 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573269 257 SLFSMDGDFAPMEELSQLRKKYGFLLVIDDAHGTFVCGENGGGVAEEFNCEADVDLCVgTLSKAAGCHGGFIACSKKWKQ 336
Cdd:PRK05937 151 SVYSFKGTLAPLEQIIALSKKYHAHLIVDEAHAMGIFGDDGKGFCHSLGYENFYAVLV-TYSKALGSMGAALLSSSEVKQ 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573269 337 LIQSRGRSFIFSTAIP--VPMAAAAYAAVVVARKEIWRRK--AIWERVKEFKELSGVDISSPIISLVVGNQEkalkASRY 412
Cdd:PRK05937 230 DLMLNSPPLRYSTGLPphLLISIQVAYDFLSQEGELARKQlfRLKEYFAQKFSSAAPGCVQPIFLPGISEQE----LYSK 305
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 42573269 413 LLKSGFHVMAIRPPTVPpnscRLRVTLSAAHTTEDVKKLITALSSCLD 460
Cdd:PRK05937 306 LVETGIRVGVVCFPTGP----FLRVNLHAFNTEDEVDILVSVLATYLE 349
|
|
| PLN02822 |
PLN02822 |
serine palmitoyltransferase |
102-455 |
3.55e-18 |
|
serine palmitoyltransferase
Pssm-ID: 178417 [Multi-domain] Cd Length: 481 Bit Score: 86.72 E-value: 3.55e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573269 102 KKLLLFSGNDYLGLSSHPTISNAAANAVKEYGMGPKGSALICGYTTYHRLLESSLAQLKKKEDCLVCPTGFAanmaamva 181
Cdd:PLN02822 109 KDVVNFASANYLGLIGNEKIKESCTSALEKYGVGSCGPRGFYGTIDVHLDCETKIAKFLGTPDSILYSYGLS-------- 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573269 182 igSVASLLAASGKplknEKVAIFSDALNHASIIDGVRLAERQgnveVFVYRHCDMYHLNSLLSNC-------KMKRKVVV 254
Cdd:PLN02822 181 --TIFSVIPAFCK----KGDIIVADEGVHWGIQNGLYLSRST----IVYFKHNDMESLRNTLEKLtaenkrkKKLRRYIV 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573269 255 TDSLFSMDGDFAPMEELSQLRKKYGFLLVIDDAHGTFVCGENGGGVAEEFNCEAD-VDLCVGTLSKAAGCHGGFIACSKK 333
Cdd:PLN02822 251 VEAIYQNSGQIAPLDEIVRLKEKYRFRVLLDESNSFGVLGKSGRGLSEHFGVPIEkIDIITAAMGHALATEGGFCTGSAR 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573269 334 W--KQLIQSRGrsFIFSTAIP----------VPMAAAAYAAVVVARKEIwrrKAIWERVKEFKELS-GVDISSPIISLVV 400
Cdd:PLN02822 331 VvdHQRLSSSG--YVFSASLPpylasaaitaIDVLEDNPSVLAKLKENI---ALLHKGLSDIPGLSiGSNTLSPIVFLHL 405
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 42573269 401 GNQEKALK---------ASRYLLKSGFHVMAIRPPTVppNSCRL----RVTLSAAHTTEDVKKLITAL 455
Cdd:PLN02822 406 EKSTGSAKedlsllehiADRMLKEDSVLVVVSKRSTL--DKCRLpvgiRLFVSAGHTESDILKASESL 471
|
|
| AAT_I |
cd01494 |
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP) ... |
152-329 |
3.47e-04 |
|
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP)-dependent enzymes. PLP combines with an alpha-amino acid to form a compound called a Schiff base or aldimine intermediate, which depending on the reaction, is the substrate in four kinds of reactions (1) transamination (movement of amino groups), (2) racemization (redistribution of enantiomers), (3) decarboxylation (removing COOH groups), and (4) various side-chain reactions depending on the enzyme involved. Pyridoxal phosphate (PLP) dependent enzymes were previously classified into alpha, beta and gamma classes, based on the chemical characteristics (carbon atom involved) of the reaction they catalyzed. The availability of several structures allowed a comprehensive analysis of the evolutionary classification of PLP dependent enzymes, and it was found that the functional classification did not always agree with the evolutionary history of these enzymes. Structure and sequence analysis has revealed that the PLP dependent enzymes can be classified into four major groups of different evolutionary origin: aspartate aminotransferase superfamily (fold type I), tryptophan synthase beta superfamily (fold type II), alanine racemase superfamily (fold type III), and D-amino acid superfamily (fold type IV) and Glycogen phophorylase family (fold type V).
Pssm-ID: 99742 [Multi-domain] Cd Length: 170 Bit Score: 41.21 E-value: 3.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573269 152 LESSLAQL--KKKEDCLVCPTGFAANMAAMVAIgsvasllaasgkpLKNEKVAIfSDALNHASIIdgVRLAERQG-NVEV 228
Cdd:cd01494 5 LEEKLARLlqPGNDKAVFVPSGTGANEAALLAL-------------LGPGDEVI-VDANGHGSRY--WVAAELAGaKPVP 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573269 229 FVYRHCDMYHLN-SLLSNCKMKRKV--VVTDSLFSMDGDFAPMEELSQLRKKYGFLLVIDDAHGTFVCGENGGGVAEEFn 305
Cdd:cd01494 69 VPVDDAGYGGLDvAILEELKAKPNValIVITPNTTSGGVLVPLKEIRKIAKEYGILLLVDAASAGGASPAPGVLIPEGG- 147
|
170 180
....*....|....*....|....*
gi 42573269 306 ceADVdlCVGTLSKA-AGCHGGFIA 329
Cdd:cd01494 148 --ADV--VTFSLHKNlGGEGGGVVI 168
|
|
| AAT_like |
cd00609 |
Aspartate aminotransferase family. This family belongs to pyridoxal phosphate (PLP)-dependent ... |
268-455 |
1.94e-03 |
|
Aspartate aminotransferase family. This family belongs to pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). Pyridoxal phosphate combines with an alpha-amino acid to form a compound called a Schiff base or aldimine intermediate, which depending on the reaction, is the substrate in four kinds of reactions (1) transamination (movement of amino groups), (2) racemization (redistribution of enantiomers), (3) decarboxylation (removing COOH groups), and (4) various side-chain reactions depending on the enzyme involved. Pyridoxal phosphate (PLP) dependent enzymes were previously classified into alpha, beta and gamma classes, based on the chemical characteristics (carbon atom involved) of the reaction they catalyzed. The availability of several structures allowed a comprehensive analysis of the evolutionary classification of PLP dependent enzymes, and it was found that the functional classification did not always agree with the evolutionary history of these enzymes. The major groups in this CD corresponds to Aspartate aminotransferase a, b and c, Tyrosine, Alanine, Aromatic-amino-acid, Glutamine phenylpyruvate, 1-Aminocyclopropane-1-carboxylate synthase, Histidinol-phosphate, gene products of malY and cobC, Valine-pyruvate aminotransferase and Rhizopine catabolism regulatory protein.
Pssm-ID: 99734 [Multi-domain] Cd Length: 350 Bit Score: 40.40 E-value: 1.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573269 268 MEELSQLRKKYGFLLVIDDAHGTFVCGENGGGVAEEFNcEADVDLCVGTLSKAAGCHG---GFIACSKKW-KQLIQSRGR 343
Cdd:cd00609 154 LEELAELAKKHGILIISDEAYAELVYDGEPPPALALLD-AYERVIVLRSFSKTFGLPGlriGYLIAPPEElLERLKKLLP 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573269 344 SFIFSTAIPV-----PMAAAAYAAVVVARKEI-WRRKAIWERVKEFKELSGVDISSPIISLVVGNQEKALKASRYLLKSg 417
Cdd:cd00609 233 YTTSGPSTLSqaaaaAALDDGEEHLEELRERYrRRRDALLEALKELGPLVVVKPSGGFFLWLDLPEGDDEEFLERLLLE- 311
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 42573269 418 FHVmAIRPPTVPPNSCR--LRVTLsaAHTTEDVKKLITAL 455
Cdd:cd00609 312 AGV-VVRPGSAFGEGGEgfVRLSF--ATPEEELEEALERL 348
|
|
| |
